C1668
Cys-Asp-Pro-Gly-Tyr-Ile-Gly-Ser-Arg amide
≥95% (HPLC)
Sinónimos:
Laminin Fragment 925-933 Amide
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About This Item
Fórmula empírica (notación de Hill):
C40H63N13O13S
Número de CAS:
Peso molecular:
966.07
UNSPSC Code:
12352200
assay
≥95% (HPLC)
contains
2-mercaptoethanol as stabilizer
storage temp.
−20°C
Storage Class
13 - Non Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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N Sakamoto et al.
Cancer research, 51(3), 903-906 (1991-02-01)
A laminin-derived synthetic peptide, Cys-Asp-Pro-Gly-Tyr-Ile-Gly-Ser-Arg-NH2 (CDPGYIGSR-H2), containing an active site for cell binding inhibited both angiogenesis and solid tumor growth. It potently suppressed both embryonic angiogenesis of the chick chorioallantoic membrane and migration of vascular endothelial cells induced by a
J R Starkey et al.
Biochimica et biophysica acta, 1429(1), 187-207 (1999-01-27)
The structure of laminin peptide 11 (CDPGYIGSR-NH2) contains valuable information for the design of mimetic compounds with anti-invasive and anti-metastatic properties. An alanine scan replacement experiment identified Tyr5, Ile6 and Arg9 residues as contributing significantly to anti-invasive activity. Circular dichroism
Jianguo Gu et al.
The Journal of biological chemistry, 277(22), 19922-19928 (2002-03-14)
Cell adhesion to the extracellular matrix inhibits apoptosis, but the molecular mechanisms underlying the signals transduced by different matrix components are not well understood. Here, we examined integrin-mediated antiapoptotic signals from laminin-10/11 in comparison with those from fibronectin, the best
G J Ostheimer et al.
The Journal of biological chemistry, 267(35), 25120-25128 (1992-12-15)
Peptide 11, CDPGYIGSR-NH2, is a segment of laminin which blocks tumor cell invasion. A high affinity laminin receptor in tumor cells is thought to be blocked by the carboxyl-terminal YIGSR, and conformational energy calculations suggest that the glycine in YIGSR
M F Champliaud et al.
Experimental cell research, 259(2), 326-335 (2000-08-31)
Laminins assemble into trimers composed of alpha, beta, and gamma chains which posttranslationally are glycosylated and sometimes proteolytically cleaved. In the current paper we set out to characterize posttranslational modifications and the laminin isoforms formed by laminin alpha1 and alpha5
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